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| | <StructureSection load='4o3x' size='340' side='right'caption='[[4o3x]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='4o3x' size='340' side='right'caption='[[4o3x]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o3x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actpl Actpl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O3X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o3x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinobacillus_pleuropneumoniae Actinobacillus pleuropneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O3X FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o3w|4o3w]], [[4o3y|4o3y]], [[4o3z|4o3z]], [[4o49|4o49]], [[4o4u|4o4u]], [[4o4x|4o4x]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4o3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o3x OCA], [https://pdbe.org/4o3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o3x RCSB], [https://www.ebi.ac.uk/pdbsum/4o3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o3x ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tbpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=715 ACTPL])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o3x OCA], [http://pdbe.org/4o3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o3x RCSB], [http://www.ebi.ac.uk/pdbsum/4o3x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o3x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0T4F6_ACTPL G0T4F6_ACTPL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actpl]] | + | [[Category: Actinobacillus pleuropneumoniae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Calmettes, C]] | + | [[Category: Calmettes C]] |
| - | [[Category: Moraes, T F]] | + | [[Category: Moraes TF]] |
| - | [[Category: Schryvers, A B]] | + | [[Category: Schryvers AB]] |
| - | [[Category: Yu, R H]] | + | [[Category: Yu RH]] |
| - | [[Category: Host pathogen interaction]]
| + | |
| - | [[Category: Iron acquisition]]
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| - | [[Category: Metal transport]]
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| - | [[Category: Structure-based vaccine design]]
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| - | [[Category: Surface lipoprotein]]
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| - | [[Category: Transferrin receptor]]
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| Structural highlights
Function
G0T4F6_ACTPL
Publication Abstract from PubMed
Host adapted Gram-negative bacterial pathogens from the Pasteurellaceae, Neisseriaceae and Moraxellaceae families normally reside in the upper respiratory or genitourinary tracts of their hosts and rely on utilizing iron from host transferrin (Tf) for growth and survival. The surface receptor proteins that mediate this critical iron acquisition pathway have been proposed as ideal vaccine targets due to the critical role that they play in survival and disease pathogenesis in vivo. In particular, the surface lipoprotein component of the receptor, Tf binding protein B (TbpB), had received considerable attention as a potential antigen for vaccines in humans and food production animals but this has not translated into the series of successful vaccine products originally envisioned. Preliminary immunization experiments suggesting that host Tf could interfere with development of the immune response prompted us to directly address this question with site-directed mutant proteins defective in binding Tf. Site-directed mutants with dramatically reduced binding of porcine transferrin and nearly identical structure to the native proteins were prepared. A mutant Haemophilus parasuis TbpB was shown to induce an enhanced B-cell and T-cell response in pigs relative to native TbpB and provide superior protection from infection than the native TbpB or a commercial vaccine product. The results indicate that binding of host transferrin modulates the development of the immune response against TbpBs and that strategies designed to reduce or eliminate binding can be used to generate superior antigens for vaccines.
Nonbinding site-directed mutants of transferrin binding protein B enhances their immunogenicity and protective capabilities.,Frandoloso R, Martinez-Martinez S, Calmettes C, Fegan J, Costa E, Curran D, Yu RH, Gutierrez-Martin CB, Rodriguez Ferri EF, Moraes TF, Schryvers AB Infect Immun. 2014 Dec 29. pii: IAI.02572-14. PMID:25547790[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Frandoloso R, Martinez-Martinez S, Calmettes C, Fegan J, Costa E, Curran D, Yu RH, Gutierrez-Martin CB, Rodriguez Ferri EF, Moraes TF, Schryvers AB. Nonbinding site-directed mutants of transferrin binding protein B enhances their immunogenicity and protective capabilities. Infect Immun. 2014 Dec 29. pii: IAI.02572-14. PMID:25547790 doi:http://dx.doi.org/10.1128/IAI.02572-14
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